Covalent modification of the nucleotide binding domains of cystic fibrosis transmembrane conductance regulator.
about
Normal gating of CFTR requires ATP binding to both nucleotide-binding domains and hydrolysis at the second nucleotide-binding domain.ADP inhibits function of the ABC transporter cystic fibrosis transmembrane conductance regulator via its adenylate kinase activity.Divergent signature motifs of nucleotide binding domains of ABC multidrug transporter, CaCdr1p of pathogenic Candida albicans, are functionally asymmetric and noninterchangeableA conditional probability analysis of cystic fibrosis transmembrane conductance regulator gating indicates that ATP has multiple effects during the gating cycle.Cysteine accessibility probes timing and extent of NBD separation along the dimer interface in gating CFTR channels.Mutating the Conserved Q-loop Glutamine 1291 Selectively Disrupts Adenylate Kinase-dependent Channel Gating of the ATP-binding Cassette (ABC) Adenylate Kinase Cystic Fibrosis Transmembrane Conductance Regulator (CFTR) and Reduces Channel Function inHuman-mouse cystic fibrosis transmembrane conductance regulator (CFTR) chimeras identify regions that partially rescue CFTR-ΔF508 processing and alter its gating defect.Covalent modification of a volatile anesthetic regulatory site activates TASK-3 (KCNK9) tandem-pore potassium channels.Insight in eukaryotic ABC transporter function by mutation analysis.On the mechanism of MgATP-dependent gating of CFTR Cl- channelsReversible silencing of CFTR chloride channels by glutathionylation.Prolonged nonhydrolytic interaction of nucleotide with CFTR's NH2-terminal nucleotide binding domain and its role in channel gating.A mutation in CFTR modifies the effects of the adenylate kinase inhibitor Ap5A on channel gating.Mutation of Walker-A lysine 464 in cystic fibrosis transmembrane conductance regulator reveals functional interaction between its nucleotide-binding domains.Structural mechanisms of CFTR function and dysfunction.Control of CFTR channel gating by phosphorylation and nucleotide hydrolysis.
P2860
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P2860
Covalent modification of the nucleotide binding domains of cystic fibrosis transmembrane conductance regulator.
description
1998 nî lūn-bûn
@nan
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
1998年论文
@zh
1998年论文
@zh-cn
name
Covalent modification of the n ...... embrane conductance regulator.
@en
Covalent modification of the n ...... embrane conductance regulator.
@nl
type
label
Covalent modification of the n ...... embrane conductance regulator.
@en
Covalent modification of the n ...... embrane conductance regulator.
@nl
prefLabel
Covalent modification of the n ...... embrane conductance regulator.
@en
Covalent modification of the n ...... embrane conductance regulator.
@nl
P2860
P356
P1476
Covalent modification of the n ...... embrane conductance regulator.
@en
P2093
P2860
P304
31873-31879
P356
10.1074/JBC.273.48.31873
P407
P577
1998-11-01T00:00:00Z